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ChemPhotoChem. 2017 Jun;1(6):256-259. doi: 10.1002/cptc.201700039. Epub 2017 Apr 13.

Saposin B Binds the Lipofuscin Bisretinoid A2E and Prevents its Enzymatic and Photooxidation.

Author information

1
Department of Chemistry, Syracuse University, Syracuse, NY 13244 (USA).
2
Department of Chemistry, State University of New York at Potsdam, Potsdam, NY 13676 (USA).
3
ICHOR Therapeutics, 2521 US-11, Lafayette, NY 13084 (USA).
4
Department of Medicine, State University of New York, Upstate Medical University, Syracuse, NY 13210 (USA).

Abstract

Vitamin A based bisretinoid accumulation is a major focus in the study of macular degeneration. Whether specific endogenous lysosomal proteins can bind A2E, a pronounced bisretinoid in lipofuscin granules in retinal pigment epithelial cells, and interfere with enzymatic or photoinduced oxidation of such, has not been explored. Herein, using fluorescence and electronic absorption spectroscopy and mass spectrometry, we demonstrate that Saposin B, a critical protein in the degradation of sulfatides and "flushing" of lipids, can bind A2E, preventing its H2O2-dependent enzymatic oxidation by horseradish peroxidase and photooxidation by blue light (λ=450-460 nm).

KEYWORDS:

bisretinoids; enzymatic oxidation; macular degeneration; photooxidation; saposin B

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